1adc



CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES

Exploring the Structure
 Alcohol dehydrogenase uses two molecular "tools" to perform its reaction on ethanol. The first is a zinc atom, which is used to hold and position the alcoholic group on ethanol. The second is a large NAD cofactor (constructed using the vitamin niacin), which actually performs the reaction. PDB entry 1adc, shown here, contains ethanol molecules bound to the two active sites. A slightly-modified version of NAD was used in the structure analysis, so that the enzyme would not immediately attack the ethanol. Notice here how the zinc atom, shown in light blue, is cradled by three amino acids from the protein: cysteine 46 to the left, cysteine 174 to the right, and histidine 67 above. The ethanol, shown in green and magenta, binds to the zinc and is positioned next to the NAD cofactor, which extends below the ethanol molecule in this illustration.

About this Structure
1ADC is a Single protein structure of sequence from Equus caballus with ZN, PAD and EOH as ligands. The following page contains interesting information on the relation of 1ADC with [Alcohol Dehydrogenase]. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.

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